Biochemical characterization of a UDP-sugar pyrophosphorylase from Thermus caldophilus GK24

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Title
Biochemical characterization of a UDP-sugar pyrophosphorylase from Thermus caldophilus GK24
Author(s)
Joong Su Kim; Suk Hoon Koh; Hyun Jae Shin; Dae Sil Lee; Se Young Lee
Bibliographic Citation
Biotechnology and Applied Biochemistry, vol. 29, pp. 11-17
Publication Year
1999
Abstract
An extremely thermostable UDP-GlcNAc pyrophosphorylase has been purified from Thermus caldophilus GK24 by chromatographic methods including ionexchange, hydrophobic interaction, and affinity chromatographies. The specific activity of the enzyme was enriched 41.8-fold, with a recovery of 2%. The molecular mass of the enzyme was 41 kDa by SDS/PAGE and 45 kDa by gel-filtration chromatography. The activity was maximum at 86°C and its half-life at 95°C was 30 min. Its optimum pH was 6.9 in the presence of Mg2+ ions. A biochemical study showed that UDP-GlcNAc pyrophosphorylase activity could be enhanced by fructose I-phosphate, a precursor of UDP-GlcNAc. The enzyme showed a broad substrate specificity with sugar I-phosphates, including glucose I-phosphate, GlcNAc-1-P and xylose I-phosphate. The enzyme was therefore named UDP-sugar pyrophosphorylase. The N-terminal and internal peptide sequences were determined and compared with known sequences from various sources. It was found that N-terminal sequence is similar to that of UDP-GlcNAc and UDP-glucose pyrophosphorylases from other bacterial sources.
ISSN
0885-4513
Publisher
Wiley
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > SME Support Center > 1. Journal Articles
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